Ammino Acids And Proteins Flashcards

1
Q

Where do humans get proteins from?

A

Foods: meats, eggs, diary and fish.

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2
Q

Where in the body are proteins found?

A

-Enzymes
-Hormones
-Collogen
-Antibodies

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3
Q

What is the polymer of proteins called?

A

Polypeptide

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3
Q

What is the monomer of proteins called?

A

Ammino acids

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4
Q

What elements do all proteins include?

A

O, H, C, N (sometimes S)

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5
Q

What groups do all proteins include in their basic structures?

A

-Amnio group
-Carboxyl group
-R group

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6
Q

What group varies in a protein structure?

A

R group- structure determines function.

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7
Q

How do humans get proteins which are not synthesised in the body?

A

Consuming foods which contain proteins and are then broken down into ammino acids (by hydrolysing) to then build more proteins.

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7
Q

What bonds are in ammino acids?

A

Peptide bond between carbon and nitrogen (very strong).

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7
Q

How many natural proteins are there?

A

20

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8
Q

How do plants absorb proteins?

A

Through nitrogen in the soil.

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9
Q

Which enzymes hydrolyses proteins?

A

Protease.

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9
Q

What does a reaction between two ammino acids from?

A

A dipeptide

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10
Q

What type of bond is a peptide bond?

A

Very strong covalent bond.

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11
Q

How are proteins produced in the body?

A

Produced from the mRNA to have the right sequence and therefore function (goes through the ribosomes, nucleus and the rough ER).

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12
Q

What is the primary structure of a protein?

A

A chain of ammino acids with peptide bonds.

12
Q

What is the secondary structure of a protein?

A

-Forms an alpha helix or a beta pleated sheet.
-Formed by folding or coiling of the primary structure.
-Has hydrogen bonds between carboxyl and ammino groups- 4 places in between.

12
Q

What is the tertiary structure of a protein?

A

-Further coiling and folding of the secondary structure.
-Has three bond: hydrogen, ionic and disulphide bridges.
-Most proteins are now functional.

13
Q

What is the quaternary structure of a protein?

A

-Contains more than one polypeptide chain.
-Very specific
-Still coiled or pleated
-Contain inorganic compounds such as iron.

14
Q

What is an example of a quaternity protein?

A

Haemoglobin.

15
Q

Disulphide bridges:

A

-Very strong
-Broken down by reducing agents
-Placement is determined by R group.
-Between any ammino acid which contain S.

16
Q

Hydrogen bonds:

A

-Broken down easily by temperature and pH as the concentration is changed.

17
Q

Ionic bonds:

A

-Formed by oxygen on carboxyl groups.
-Between positive and negatively charged elements.

18
Q

How do globular proteins form?

A

-Hydrophobic parts of the R group move to the centre of the polypeptide to avid water.
-Hydrophilic parts move towards the water.
-Causes twisting of the ammino acid chain and changes shape.

19
How is the tertiary structure denatured?
By heating -Increases kinetic energy so parts vibrate faster. -Bonds are broken(not covalent) and the structure begins to untwist.
20
What extra group does the quaternary structure have?
A prosthetic group that helps it perform its function.
21
What are the two types of proteins?
Globular and Fiberous.
22
What are the features of fibrous proteins?
-Has three polypeptide chain (triple helix) -Has structural functions. -Repetitive structure -Insoluble in water -Has hydrogen bonds. -Has a long and thin shape
23
What are the features of globular proteins?
-Has 4 polypeptide chains (2 alpha, 2 beta) -Has a spherical structure -Functional proteins -Soluble in water -Has the three types of bonds